Department of Cell Biology, Pat and Jim Calhoun Center for Cardiology, University of Connecticut Health Center, Farmington, CT 06030, USA.
J Cardiovasc Pharmacol. 2011 Oct;58(4):354-62. doi: 10.1097/FJC.0b013e31821e5649.
Directed protein phosphorylation is indisputably critical for a multitude of cellular processes. A growing body of research demonstrates A kinase anchoring proteins (AKAPs) to mediate a significant number of phosphorylation events in the heart. By acting as molecular tethers for the regulatory subunit of protein kinase A, AKAPs focus kinase activity onto specific substrate. In the time since their discovery, the AKAP model has evolved in appreciation of the broader role these scaffolds play in coordinating multiple signaling enzymes to efficiently regulate dynamic cellular processes. The focus of this review is on the emerging role of AKAPs in regulating the 3 main cardiac phosphatases: Protein Phosphatase 1 by AKAP18 and Yotiao, and Protein Phosphatases 2A and 2B by muscle specific A-kinase anchoring protein.
蛋白的定向磷酸化对多种细胞过程至关重要。越来越多的研究表明,蛋白激酶锚定蛋白(AKAPs)在心脏中介导了大量的磷酸化事件。作为蛋白激酶 A 的调节亚基的分子连接物,AKAPs 将激酶活性集中在特定的底物上。自发现以来,AKAP 模型不断发展,以更好地理解这些支架在协调多种信号酶以有效调节动态细胞过程中的更广泛作用。本综述的重点是 AKAP 在调节 3 种主要的心肌磷酸酶中的新作用:AKAP18 和 Yotiao 调节蛋白磷酸酶 1,以及肌肉特异性 AKAP 调节蛋白磷酸酶 2A 和 2B。